Abstract:
:The SecY protein of Escherichia coli is an integral membrane component of the protein export apparatus. Suppressor mutations in the secY gene (prlA alleles) have been isolated that restore the secretion of precursor proteins with defective signal sequences. These mutations have never been shown to affect the translocation of wild-type precursor proteins. Here, we report that prlA suppressor mutations relieve the proton-motive force (pmf) dependency of the translocation of wild-type precursors, both in vivo and in vitro. Furthermore, the proton-motive force dependency of the translocation of a precursor with a stably folded domain in the mature region was suppressed by prlA mutations in vitro. These data show that prlA mutations cause a general relaxation of the export apparatus rather than a specific change that results in bypassing of the recognition of the signal sequence. In addition, these results are indicative for a mechanism in which the proton-motive force stimulates translocation by altering the conformation of the translocon.
journal_name
Proc Natl Acad Sci U S Aauthors
Nouwen N,de Kruijff B,Tommassen Jdoi
10.1073/pnas.93.12.5953subject
Has Abstractpub_date
1996-06-11 00:00:00pages
5953-7issue
12eissn
0027-8424issn
1091-6490journal_volume
93pub_type
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